文献类型： 外文期刊
第一作者： Xia, Ruixue
作者： Xia, Ruixue;Lu, Yang;Wang, Na;Zhang, Anqi;Guo, Changyou;Xu, Zhenmei;He, Yuanzheng;Sun, Mingxia;Cai, Xuehui;He, Yuanzheng
作者机构：
关键词： Heliorhodopsin; Acetate; Nanobody; Cryo-EM
期刊名称：BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS （ 影响因子：2.2； 五年影响因子：2.5 ）
ISSN： 0006-291X
年卷期： 2025 年 750 卷
页码：
收录情况： SCI
摘要： Heliorhodopsins (HeRs) represent a distinct class of microbial rhodopsins (MRs) with an inverted membrane topology compared to other MRs. Previous structural studies have shown that HeRs lack a proton acceptor residue, and protons are never released from the protein. In this study, we present the cryo-electron microscopy (cryo-EM) structure of HeR bound to a nanobody. The structure reveals an acetate-like molecule in the Schiff base cavity (SBC) on the intracellular side of HeR under neutral condition. Structural comparisons and analyses suggest that the acetate molecule may function as a proton acceptor for the protonated retinal Schiff base (RSB) and act as a mediator for the intramolecular signaling transduction in HeR during light stimulation. These structural insights shed new light on the mechanism and function of HeR.
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